Zobrazeno 1 - 10
of 82
pro vyhledávání: '"Ortwin Meyer"'
Autor:
Tobias Maisel, Stephanie Joseph, Thorsten Mielke, Jörg Bürger, Stephan Schwarzinger, Ortwin Meyer
Publikováno v:
PLoS ONE, Vol 7, Iss 10, p e47424 (2012)
CoxD of the α-proteobacterium Oligotropha carboxidovorans is a membrane protein which is involved in the posttranslational biosynthesis of the [CuSMoO₂] cluster in the active site of the enzyme CO dehydrogenase. The bacteria synthesize CoxD only i
Externí odkaz:
https://doaj.org/article/8392b082e89742deb83b63f4e15351ae
Publikováno v:
BioMetals. 23:613-622
Soluble ammonia monooxygenase (AMO) from Nitrosomonas europaea was purified to homogeneity and metals in the active sites of the enzyme (Cu, Fe) were analyzed by electron paramagnetic resonance (EPR) spectroscopy. EPR spectra were obtained for a type
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f673038f334509d245432c64c9db9d6
https://doi.org/10.1007/s10534-010-9308-2
https://doi.org/10.1007/s10534-010-9308-2
Publikováno v:
bchm. 390:863-873
Ammonia monooxygenase (AMO) of Nitrosomonas europaea is a metalloenzyme that catalyzes the oxidation of ammonia to hydroxylamine. This study shows that AMO resides in the cytoplasm of the bacteria in addition to its location in the membrane and is di
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e5767807525cbbf30546b146d03a1c4
https://doi.org/10.1515/bc.2009.085
https://doi.org/10.1515/bc.2009.085
Publikováno v:
Microbiology. 155:279-284
The ammonia monooxygenase (AMO) ofNitrosomonas europaeais a metalloenzyme that catalyses the oxidation of ammonia to hydroxylamine. We have identified histidine 191 of AmoA as the binding site for the oxidized mechanism-based inactivator acetylene. B
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2cc09aa58ae55cb9c8faf9d92971ac3
https://doi.org/10.1099/mic.0.023721-0
https://doi.org/10.1099/mic.0.023721-0
Publikováno v:
Microbial Physiology. 16:187-197
Nitrosomonas europaea can grow under conditions of chemolithoautotrophic aerobic (oxygen as oxidant) as well as anaerobic [nitrogen dioxide (NO2) as oxidant] nitrification or chemoorganotrophic anaerobic pyruvate-dependent denitrification. In this st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6590d6287540f7092586d8926cea5741
https://doi.org/10.1159/000142531
https://doi.org/10.1159/000142531
Publikováno v:
FEMS Microbiology Letters. 273:260-267
Ammonium transporters form a conserved family of transport proteins and are widely distributed among all domains of life. The genome of Nitrosomonas europaea codes for a single gene (rh1) that belongs to the family of the AMT/Rh ammonium transporters
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd339f139cbf6b7557253cbf91b8369f
https://doi.org/10.1111/j.1574-6968.2007.00805.x
https://doi.org/10.1111/j.1574-6968.2007.00805.x
Autor:
Ortwin Meyer, Jörg Tachil
Publikováno v:
FEMS Microbiology Letters. 148:203-208
The redox state of molybdopterin cytosine dinucleotide (MCD) from the molybdo-iron-sulfur-flavoprotein CO dehydrogenase of the carboxidotrophic bacterium Hydrogenophaga pseudoflava has been studied. MCD has been purified as the dicarboxamidomethylate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::507fd5d90ae2800ee140f54d659feda9
https://doi.org/10.1111/j.1574-6968.1997.tb10289.x
https://doi.org/10.1111/j.1574-6968.1997.tb10289.x
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 10:518-528
Carbon monoxide dehydrogenase from the bacterium Oligotropha carboxidovorans catalyzes the oxidation of CO to CO(2) at a unique [CuSMoO(2)] cluster. In the bacteria the cluster is assembled post-translational. The integration of S, and particularly o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1271f3793b6f10d5b47c4b6f0c8bcbf
https://doi.org/10.1007/s00775-005-0006-4
https://doi.org/10.1007/s00775-005-0006-4
Publikováno v:
Proceedings of the National Academy of Sciences. 99:15971-15976
The CO dehydrogenase of the eubacterium Oligotropha carboxidovorans is a 277-kDa Mo- and Cu-containing iron-sulfur flavoprotein. Here, the enzyme's active site in the oxidized or reduced state, after inactivation with potassium cyanide or with n-buty
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8be32b75a048b45000f4d7dd73562917
https://doi.org/10.1073/pnas.212640899
https://doi.org/10.1073/pnas.212640899
Publikováno v:
Journal of Molecular Biology. 301:1221-1235
Crystal structures of carbon monoxide dehydrogenase (CODH), a seleno-molybdo-iron-sulfur flavoprotein from the aerobic carbon monoxide utilizing carboxidotrophic eubacterium Hydrogenophaga pseudoflava, have been determined from the enzyme synthesized
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da35160d1dd2dec8ea94c02c41041717
https://doi.org/10.1006/jmbi.2000.4023
https://doi.org/10.1006/jmbi.2000.4023